› 1yhw

X-ray diffraction
1.8Å resolution

Crystal Structure of PAK1 kinase domain with one point mutations (K299R)

Released:
DOI: 10.2210/pdb1yhw/pdb
PDB entry 1yhw coloured by chain, front view.
PDB entry 1yhw coloured by chain, side view.
PDB entry 1yhw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The active conformation of the PAK1 kinase domain.
Lei M, Robinson MA, Harrison SC
Structure 13 769-78 (2005)
PMID: 15893667

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase PAK 1 Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 33.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13153 (Residues: 249-545; Coverage: 55%)
Gene name: PAK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2221
Unit cell:
a: 51.763Å b: 103.049Å c: 122.639Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.226 0.244
Expression system: Escherichia coli

Quick links

Citations

15 review citations

The structural basis for control of eukaryotic protein kinases.
Endicott et al. (2012)
14 more

7 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
6 more